Electrochemical Crystallization for Recovery of Phosphorus and Potassium from Urine as K-Struvite, with A Sacrificial Magnesium Anode

Declining earth resources, rising ore cost and pollution call for better recycling of wastewater in the context of the circular economy. In particular, urine is a potential huge source of phosphorus (P) and potassium (K) agricultural nutrients, yet the efficiency of actual methods for P and K recovery are limited. Here we designed a electrochemical crystallization system using sacrificial magnesium anodes to recover P and K in the form of K-struvite (MgKPO4·6H2O) from simulated urine at low (P/K=0.25) and high (P/K=0.6) phosphate levels, respectively. Results show optimal recoveries of 88.5% for P and 35.4% for K in the form of rod-shaped K-struvite at 3.5 mA/cm2, yet higher current density reduced recovery due to side reactions and pH increase. Adding phosphate to urine increased K recovery to 35.4% versus 15.0% without phosphate. Adding prefabricated struvite crystals at 1.6 g/L into urine enhanced the recovery of K by 14.7% and of P by 23.7% compared to the control group. Overall, our findings show that electrochemical crystallization is promising for the recovery of K-struvite fertilizers.

Performance improvement of a crystallization system through optimization and sensitivity analysis

PurposeThis paper deals with the performance optimization and sensitivity analysis for crystallization system of a sugar plant.Design/methodology/approachCrystallization system comprises of five subsystems, namely crystallizer, centrifugal pump and sugar grader. The Chapman–Kolmogorov differential equations are derived from the transition diagram of the crystallization system using mnemonic rule. These equations are solved to compute reliability and steady state availability by putting the appropriate combinations of failure and repair rates using normalizing and initial boundary conditions. The performance optimization is carried out by varying number of generations, population size, crossover and mutation probabilities. Finally, sensitivity analysis is performed to analyze the effect of change in failure rates of each subsystem on availability, mean time to failure (MTBF) and mean time to repair (MTTR).FindingsThe highest performance observed is 96.95% at crossover probability of 0.3 and sugar grader subsystem comes out to be the most critical and sensitive subsystem.Originality/valueThe findings of the paper highlights the optimum value of performance level at failure and repair rates for subsystems and also helps identify the most sensitive subsystem. These findings are highly beneficial for the maintenance personnel of the plant to plan the maintenance strategies accordingly.

Crystal structures of human ENPP1 in apo and bound forms

Cancer is one of the leading causes of mortality in humans, and recent work has focused on the area of immuno-oncology, in which the immune system is used to specifically target cancerous cells. Ectonucleotide pyrophosphatase/phosphodiesterase 1 (ENPP1) is an emerging therapeutic target in human cancers owing to its role in degrading cyclic GMP-AMP (cGAMP), an agonist of the stimulator of interferon genes (STING). The available structures of ENPP1 are of the mouse enzyme, and no structures are available with anything other than native nucleotides. Here, the first X-ray crystal structures of the human ENPP1 enzyme in an apo form, with bound nucleotides and with two known inhibitors are presented. The availability of these structures and a robust crystallization system will allow the development of structure-based drug-design campaigns against this attractive cancer therapeutic target.

Monitoring the Production of High Diffraction-Quality Crystals of Two Enzymes in Real Time Using In Situ Dynamic Light Scattering

The reproducible preparation of well-diffracting crystals is a prerequisite for every structural study based on crystallography. An instrument called XtalController has recently been designed that allows the monitoring of crystallization assays using dynamic light scattering and microscopy, and integrates piezo pumps to alter the composition of the mother liquor during the experiment. We have applied this technology to study the crystallization of two enzymes, the CCA-adding enzyme of the psychrophilic bacterium Planococcus halocryophilus, and the lysozyme from hen egg white in the presence of a synthetic chemical nucleant. We were able to (i) detect early nucleation events and (ii) drive the crystallization system (through cycles of dissolution/crystallization) toward growth conditions yielding crystals with excellent diffraction properties. This technology opens a way to the rational production of samples for crystallography, ranging from nanocrystals for electron diffraction, microcrystals for serial or conventional X-ray diffraction, to larger crystals for neutron diffraction.

Monitoring the production of high diffraction-quality crystals of two enzymes in real time using in situ dynamic light scattering

ABSTRACTThe reproducible preparation of well diffracting crystals is a prerequisite for every structural study based on crystallography. An instrument called the XtalController has recently been designed that allows the monitoring of crystallization assays using dynamic light scattering and microscopy, and integrates piezo pumps to alter the composition of the mother liquor during the experiment. We have applied this technology to study the crystallization of two enzymes, the CCA-adding enzyme of the psychrophilic bacterium Planococcus halocryophilus and the hen egg white lysozyme in the presence of a synthetic chemical nucleant. We were able to i) detect early nucleation events and ii) drive the crystallization system (through cycles of dissolution/crystallization) towards growth conditions yielding crystals with excellent diffraction properties. This technology opens a way to the rational production of samples for crystallography, ranging from nanocrystals for electron diffraction, microcrystals for serial or conventional X-ray diffraction, to larger crystals for neutron diffraction.